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  • Schechter, Matthew A., Michael K. H. Hsieh, Linda W. Njoroge, J Will Thompson, Erik J. Soderblom, Bryan J. Feger, Constantine D. Troupes, et al. “Phosphoproteomic profiling of human myocardial tissues distinguishes ischemic from non-ischemic end stage heart failure.” PLoS One 9, no. 8 (2014): e104157. https://doi.org/10.1371/journal.pone.0104157.
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  • Huynh, Frank K., Kathleen A. Hershberger, and Matthew D. Hirschey. “Targeting sirtuins for the treatment of diabetes.” Diabetes Manag (Lond) 3, no. 3 (May 1, 2013): 245–57. https://doi.org/10.2217/dmt.13.6.
  • Merksamer, Philip I., Yufei Liu, Wenjuan He, Matthew D. Hirschey, Danica Chen, and Eric Verdin. “The sirtuins, oxidative stress and aging: an emerging link.” Aging (Albany NY) 5, no. 3 (March 2013): 144–50. https://doi.org/10.18632/aging.100544.
  • Green, Michelle F., and Matthew D. Hirschey. “SIRT3 weighs heavily in the metabolic balance: a new role for SIRT3 in metabolic syndrome.” J Gerontol A Biol Sci Med Sci 68, no. 2 (February 2013): 105–7. https://doi.org/10.1093/gerona/gls132.
  • Gut, Philipp, Bernat Baeza-Raja, Olov Andersson, Laura Hasenkamp, Joseph Hsiao, Daniel Hesselson, Katerina Akassoglou, Eric Verdin, Matthew D. Hirschey, and Didier Y. R. Stainier. “Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism.” Nat Chem Biol 9, no. 2 (February 2013): 97–104. https://doi.org/10.1038/nchembio.1136.
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  • Hershberger, Kathleen A., Jonathan Motley, Matthew D. Hirschey, and Kristin A. Anderson. “Generating mammalian sirtuin tools for protein-interaction analysis.” Methods Mol Biol 1077 (2013): 69–78. https://doi.org/10.1007/978-1-62703-637-5_5.
  • Wang, Dongning, Michelle F. Green, Eoin McDonnell, and Matthew D. Hirschey. “Oxygen flux analysis to understand the biological function of sirtuins.” Methods Mol Biol 1077 (2013): 241–58. https://doi.org/10.1007/978-1-62703-637-5_16.
  • Gut, P., B. Baeza-Raja, O. Andersson, L. Hasenkamp, J. Hsiao, D. Hesselson, K. Akassoglou, E. Verdin, M. D. Hirschey, and D. Y. R. Stainier. “Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism.” Nature Chemical Biology 9, no. 2 (2013): 97–104. https://doi.org/10.1038/nchembio.1136.
  • Fritz, Kristofer S., Michelle F. Green, Dennis R. Petersen, and Matthew D. Hirschey. “Ethanol metabolism modifies hepatic protein acylation in mice.” PLoS One 8, no. 9 (2013): e75868. https://doi.org/10.1371/journal.pone.0075868.
  • Haas, Joel T., Ji Miao, Dipanjan Chanda, Yanning Wang, Enpeng Zhao, Mary E. Haas, Matthew Hirschey, et al. “Hepatic insulin signaling is required for obesity-dependent expression of SREBP-1c mRNA but not for feeding-dependent expression.” Cell Metab 15, no. 6 (June 6, 2012): 873–84. https://doi.org/10.1016/j.cmet.2012.05.002.
  • Fritz, Kristofer S., James J. Galligan, Matthew D. Hirschey, Eric Verdin, and Dennis R. Petersen. “Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.” J Proteome Res 11, no. 3 (March 2, 2012): 1633–43. https://doi.org/10.1021/pr2008384.
  • Streeper, Ryan S., Carrie A. Grueter, Nathan Salomonis, Sylvaine Cases, Malin C. Levin, Suneil K. Koliwad, Ping Zhou, Mattew D. Hirschey, Eric Verdin, and Robert V. Farese. “Deficiency of the lipid synthesis enzyme, DGAT1, extends longevity in mice.” Aging (Albany NY) 4, no. 1 (January 2012): 13–27. https://doi.org/10.18632/aging.100424.
  • Anderson, Kristin A., and Matthew D. Hirschey. “Mitochondrial protein acetylation regulates metabolism.” Essays Biochem 52 (2012): 23–35. https://doi.org/10.1042/bse0520023.
  • Hirschey, Matthew D. “Old enzymes, new tricks: sirtuins are NAD(+)-dependent de-acylases.” Cell Metab 14, no. 6 (December 7, 2011): 718–19. https://doi.org/10.1016/j.cmet.2011.10.006.
  • Fritz, Kristofer S., James J. Galligan, Matthew D. Hirschey, Eric Verdin, and Dennis R. Petersen. “Mitochondrial Acetylomic Analysis in a Mouse Model of Alcohol-Induced Liver Injury Utilizing SIRT3 Knockout Mice.” Free Radical Biology and Medicine 51 (November 2011): S19–20. https://doi.org/10.1016/j.freeradbiomed.2011.10.044.
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  • Jing, Enxuan, Brice Emanuelli, Matthew D. Hirschey, Jeremie Boucher, Kevin Y. Lee, David Lombard, Eric M. Verdin, and C Ronald Kahn. “Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production.” Proc Natl Acad Sci U S A 108, no. 35 (August 30, 2011): 14608–13. https://doi.org/10.1073/pnas.1111308108.
  • Hirschey, Matthew D., Tadahiro Shimazu, John A. Capra, Katherine S. Pollard, and Eric Verdin. “SIRT1 and SIRT3 deacetylate homologous substrates: AceCS1,2 and HMGCS1,2.” Aging (Albany NY) 3, no. 6 (June 2011): 635–42. https://doi.org/10.18632/aging.100339.
  • Hirschey, M. D., T. Shimazu, J. -. Y. Huang, B. Schwer, and E. Verdin. “SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism.” Cold Spring Harb Symp Quant Biol 76 (2011): 267–77. https://doi.org/10.1101/sqb.2011.76.010850.
  • Verdin, Eric, Matthew D. Hirschey, Lydia W. S. Finley, and Marcia C. Haigis. “Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling.” Trends Biochem Sci 35, no. 12 (December 2010): 669–75. https://doi.org/10.1016/j.tibs.2010.07.003.
  • Qiu, Xiaolei, Katharine Brown, Matthew D. Hirschey, Eric Verdin, and Danica Chen. “Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation.” Cell Metab 12, no. 6 (December 1, 2010): 662–67. https://doi.org/10.1016/j.cmet.2010.11.015.
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  • Huang, Jing-Yi, Matthew D. Hirschey, Tadahiro Shimazu, Linh Ho, and Eric Verdin. “Mitochondrial sirtuins.” Biochim Biophys Acta 1804, no. 8 (August 2010): 1645–51. https://doi.org/10.1016/j.bbapap.2009.12.021.
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  • Shimazu, Tadahiro, Matthew D. Hirschey, Jing-Yi Huang, Linh T. Y. Ho, and Eric Verdin. “Acetate metabolism and aging: An emerging connection.” Mech Ageing Dev 131, no. 7–8 (2010): 511–16. https://doi.org/10.1016/j.mad.2010.05.001.
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  • Hirschey, Matthew D., Yong-Jin Han, Galen D. Stucky, and Alison Butler. “Imaging Escherichia coli using functionalized core/shell CdSe/CdS quantum dots.” J Biol Inorg Chem 11, no. 5 (July 2006): 663–69. https://doi.org/10.1007/s00775-006-0116-7.
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